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Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein (DPOR subunit L) (LI-POR subunit L) (EC 1.3.7.7)

 G8IUH8_PINRO            Unreviewed;       291 AA.
G8IUH8;
25-JAN-2012, integrated into UniProtKB/TrEMBL.
25-JAN-2012, sequence version 1.
28-MAR-2018, entry version 34.
RecName: Full=Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein {ECO:0000256|HAMAP-Rule:MF_00355};
Short=DPOR subunit L {ECO:0000256|HAMAP-Rule:MF_00355};
Short=LI-POR subunit L {ECO:0000256|HAMAP-Rule:MF_00355};
EC=1.3.7.7 {ECO:0000256|HAMAP-Rule:MF_00355};
Name=chlL {ECO:0000256|HAMAP-Rule:MF_00355,
ECO:0000313|EMBL:AET45849.1};
ORFNames=PCL_12666 {ECO:0000313|EMBL:AET45849.1};
Pinus roxburghii (Chir pine).
Plastid; Chloroplast {ECO:0000313|EMBL:AET45849.1}.
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Pinidae; Pinales; Pinaceae; Pinus; Pinus.
NCBI_TaxID=71650 {ECO:0000313|EMBL:AET45849.1};
[1] {ECO:0000313|EMBL:AET45849.1}
NUCLEOTIDE SEQUENCE.
STRAIN=ROXB04 {ECO:0000313|EMBL:AET45849.1};
PubMed=22731878; DOI=10.1186/1471-2148-12-100;
Parks M., Cronn R., Liston A.;
"Separating the wheat from the chaff: mitigating the effects of noise
in a plastome phylogenomic data set from Pinus L. (Pinaceae).";
BMC Evol. Biol. 12:100-100(2012).
-!- FUNCTION: Component of the dark-operative protochlorophyllide
reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce
ring D of protochlorophyllide (Pchlide) to form chlorophyllide a
(Chlide). This reaction is light-independent. The L component
serves as a unique electron donor to the NB-component of the
complex, and binds Mg-ATP. {ECO:0000256|HAMAP-Rule:MF_00355}.
-!- CATALYTIC ACTIVITY: Protochlorophyllide a + reduced ferredoxin + 2
ATP + 2 H(2)O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2
phosphate. {ECO:0000256|HAMAP-Rule:MF_00355}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000256|HAMAP-Rule:MF_00355};
Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000256|HAMAP-
Rule:MF_00355};
-!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
biosynthesis (light-independent). {ECO:0000256|HAMAP-
Rule:MF_00355}.
-!- SUBUNIT: Homodimer. Protochlorophyllide reductase is composed of
three subunits; ChlL, ChlN and ChlB. {ECO:0000256|HAMAP-
Rule:MF_00355}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
Rule:MF_00355}.
-!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
{ECO:0000256|HAMAP-Rule:MF_00355, ECO:0000256|RuleBase:RU003688}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00355}.
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EMBL; JN854162; AET45849.1; -; Genomic_DNA.
UniPathway; UPA00670; -.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro.
GO; GO:0016636; F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor; IEA:UniProtKB-UniRule.
GO; GO:0036068; P:light-independent chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
CDD; cd02032; Bchl_like; 1.
HAMAP; MF_00355; ChlL_BchL; 1.
InterPro; IPR030655; NifH/chlL_CS.
InterPro; IPR000392; NifH/frxC.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005971; Protochlorophyllide_ATP-bd.
PANTHER; PTHR42864; PTHR42864; 1.
PANTHER; PTHR42864:SF1; PTHR42864:SF1; 1.
Pfam; PF00142; Fer4_NifH; 1.
PIRSF; PIRSF000363; Nitrogenase_iron; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01281; DPOR_bchL; 1.
PROSITE; PS00746; NIFH_FRXC_1; 1.
PROSITE; PS00692; NIFH_FRXC_2; 1.
PROSITE; PS51026; NIFH_FRXC_3; 1.
3: Inferred from homology;
4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00355,
ECO:0000256|RuleBase:RU003688};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00355,
ECO:0000256|RuleBase:RU003688};
Chlorophyll biosynthesis {ECO:0000256|HAMAP-Rule:MF_00355};
Chloroplast {ECO:0000313|EMBL:AET45849.1};
Iron {ECO:0000256|HAMAP-Rule:MF_00355, ECO:0000256|RuleBase:RU003688};
Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00355,
ECO:0000256|RuleBase:RU003688};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00355};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00355,
ECO:0000256|RuleBase:RU003688};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00355,
ECO:0000256|RuleBase:RU003688};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00355,
ECO:0000256|RuleBase:RU003688};
Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00355};
Plastid {ECO:0000313|EMBL:AET45849.1}.
NP_BIND 10 15 ATP. {ECO:0000256|HAMAP-Rule:MF_00355}.
NP_BIND 180 181 ATP. {ECO:0000256|HAMAP-Rule:MF_00355}.
METAL 14 14 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00355}.
METAL 95 95 Iron-sulfur (4Fe-4S); shared with dimeric
partner. {ECO:0000256|HAMAP-
Rule:MF_00355}.
METAL 129 129 Iron-sulfur (4Fe-4S); shared with dimeric
partner. {ECO:0000256|HAMAP-
Rule:MF_00355}.
BINDING 39 39 ATP. {ECO:0000256|HAMAP-Rule:MF_00355}.
SEQUENCE 291 AA; 31728 MW; 9FC605C7CC23D7D6 CRC64;
MKIAVYGKGG IGKSTTSCNI SVALARRGQK VLQIGCDPKH DSTFTLTGFL IPTIIDTLQS
KDYHYEDIWP EDVIHKGYGG VDCVEAGGPP AGAGCGGYVV GETVKLLKEL NAFYEYDIIL
FDVLGDVVCG GFAAPLNYAD YCVIITDNGF DALFAANRIT ASIREKARTH PLRLAGLVGN
RTSRRDLINK YVEACPMPVI EVLPIIEDIR VSRVKGKTLF EMVGSEPSLN YVCNYYLGIA
DQILSQPEGI VPKEIPDREL FSLLSDLYLN PIGGGGQKKN NKENLLGFTR I


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